The programming of cell function at the transcriptional level during ovarian development and growth requires control mechanisms in which cyclic AMP and cyclic AMP-dependent protein kinases are believed to be actively involved. The function of cellular proteins may be altered or modulated through the action of cyclic AMP-dependent protein kinases which are under control by gonadotropins through the action of cyclic AMP. This research is designed to elucidate the effects of FSH and/or LH on the ontogeny of cytoplasmic and nuclear cyclic AMP-dependent protein kinases and the effects of these protein kinases on the phosphorylation of nuclear proteins during postnatal ovarian development in the rat. We aim to determine (a) the rate of biosynthesis of ovarian cytoplasmic and nuclear cyclic AMP-dependent protein kinases; (b) endogenous activation patterns of cyclic AMP-dependent protein kinases during postnatal development by endogenous gonadotropins; (c) the translocation of cytoplasmic cyclic AMP-dependent protein kinase to chromatin acceptor sites; (d) phosphorylation patterns of nuclear proteins as the consequence of protein kinase translocation; and (e) the degree of in vivo phosphorylation and dephosphorylation of ovarian RNA polymerase II by protein kinase.